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HEADER TRANSPORT PROTEIN 07-JUN-06 2H8D TITLE CRYSTAL STRUCTURE OF DEOXY HEMOGLOBIN FROM TREMATOMUS TITLE 2 BERNACCHII AT PH 8.4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN ALPHA SUBUNIT; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: HEMOGLOBIN ALPHA CHAIN, ALPHA-GLOBIN; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMOGLOBIN BETA SUBUNIT; COMPND 7 CHAIN: B, D; COMPND 8 SYNONYM: HEMOGLOBIN BETA CHAIN, BETA-GLOBIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PAGOTHENIA BERNACCHII; SOURCE 3 ORGANISM_COMMON: FISH; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: PAGOTHENIA BERNACCHII; SOURCE 6 ORGANISM_COMMON: FISH KEYWDS ROOT EFFECT, PH, COOPERATIVITY, HEMOGLOBIN, ALLOSTERY, HIGH KEYWDS 2 RESOLUTION EXPDTA X-RAY DIFFRACTION AUTHOR L.MAZZARELLA,A.VERGARA,L.VITAGLIANO,A.MERLINO,G.BONOMI, AUTHOR 2 S.SCALA,C.VERDE,G.DI PRISCO REVDAT 2 10-OCT-06 2H8D 1 JRNL REVDAT 1 29-AUG-06 2H8D 0 JRNL AUTH L.MAZZARELLA,A.VERGARA,L.VITAGLIANO,A.MERLINO, JRNL AUTH 2 G.BONOMI,S.SCALA,C.VERDE,G.DI PRISCO JRNL TITL HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXY JRNL TITL 2 HEMOGLOBIN FROM TREMATOMUS BERNACCHII AT DIFFERENT JRNL TITL 3 PH VALUES: THE ROLE OF HISTIDINE RESIDUES IN JRNL TITL 4 MODULATING THE STRENGTH OF THE ROOT EFFECT. JRNL REF PROTEINS V. 65 490 2006 JRNL REFN ASTM PSFGEY US ISSN 0887-3585 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.MAZZARELLA,G.BONOMI,M.C.LUBRANO,A.MERLINO, REMARK 1 AUTH 2 A.RICCIO,A.VERGARA,L.VITAGLIANO,C.VERDE,G.DI PRISCO REMARK 1 TITL MINIMAL STRUCTURAL REQUIREMENTS FOR ROOT EFFECT: REMARK 1 TITL 2 CRYSTAL STRUCTURE OF THE CATHODIC HEMOGLOBIN REMARK 1 TITL 3 ISOLATED FROM THE ANTARCTIC FISH TREMATOMUS NEWNESI REMARK 1 REF PROTEINS V. 62 316 2006 REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 REMARK 1 REFERENCE 2 REMARK 1 AUTH L.MAZZARELLA,R.D'AVINO,G.DI PRISCO,C.SAVINO, REMARK 1 AUTH 2 L.VITAGLIANO,P.C.E.MOODY,A.ZAGARI REMARK 1 TITL CRYSTAL STRUCTURE OF TREMATOMUS NEWNESI REMARK 1 TITL 2 HAEMOGLOBIN RE-OPENS THE ROOT EFFECT QUESTION REMARK 1 REF J.MOL.BIOL. V. 287 897 1999 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.78 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.78 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.182 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.180 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.224 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3303 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 63164 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4488 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 174 REMARK 3 SOLVENT ATOMS : 378 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL REMARK 3 NUMBER OF RESTRAINTS : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.013 REMARK 3 ANGLE DISTANCES (A) : 1.900 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: NULL REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: CRYSTALS USED FOR STRUCTURE REMARK 3 DETERMINATION PRESENT PSEUDO-MEROHEDRAL TWINNING REMARK 4 REMARK 4 2H8D COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB038057. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-OCT-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.40 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ELETTRA REMARK 200 BEAMLINE : 5.2R REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63164 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.6 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.69 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: DEOXY-HBTB 8-9.5 MG/ML MIXED WITH REMARK 280 EQUAL AMOUNT OF 7-12 % W/V PEG 6000, PBS 100 MM, KCL 0.3 M, PH REMARK 280 8.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,1/2+Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 47.31500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 OD2 ASP C 75 K K 1001 1.93 REMARK 500 OD2 ASP A 75 K K 1002 2.13 REMARK 500 K K 1002 O HOH 1378 2.13 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 NE2 HIS B 17 K K 1001 1556 1.97 REMARK 500 OD1 ASP D 13 K K 1002 1455 2.09 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2AA1 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE CATHODIC HEMOLGLOBIN ISOLATED FROM REMARK 900 THE ANTARCTIC FISH TREMATOMUS NEWNESI REMARK 900 RELATED ID: 2H8F RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF DEOXY HEMOGLOBIN FROM TREMATOMUS REMARK 900 BERNACCHII AT PH 6.2 DBREF 2H8D A 1 142 UNP P80043 HBA_PAGBE 1 142 DBREF 2H8D C 1 142 UNP P80043 HBA_PAGBE 1 142 DBREF 2H8D B 1 146 UNP P80044 HBB_PAGBE 1 146 DBREF 2H8D D 1 146 UNP P80044 HBB_PAGBE 1 146 SEQRES 1 A 142 SER LEU SER ASP LYS ASP LYS ALA ALA VAL ARG ALA LEU SEQRES 2 A 142 TRP SER LYS ILE GLY LYS SER ALA ASP ALA ILE GLY ASN SEQRES 3 A 142 ASP ALA LEU SER ARG MET ILE VAL VAL TYR PRO GLN THR SEQRES 4 A 142 LYS THR TYR PHE SER HIS TRP PRO ASP VAL THR PRO GLY SEQRES 5 A 142 SER PRO HIS ILE LYS ALA HIS GLY LYS LYS VAL MET GLY SEQRES 6 A 142 GLY ILE ALA LEU ALA VAL SER LYS ILE ASP ASP LEU LYS SEQRES 7 A 142 THR GLY LEU MET GLU LEU SER GLU GLN HIS ALA TYR LYS SEQRES 8 A 142 LEU ARG VAL ASP PRO ALA ASN PHE LYS ILE LEU ASN HIS SEQRES 9 A 142 CYS ILE LEU VAL VAL ILE SER THR MET PHE PRO LYS GLU SEQRES 10 A 142 PHE THR PRO GLU ALA HIS VAL SER LEU ASP LYS PHE LEU SEQRES 11 A 142 SER GLY VAL ALA LEU ALA LEU ALA GLU ARG TYR ARG SEQRES 1 B 146 VAL GLU TRP THR ASP LYS GLU ARG SER ILE ILE SER ASP SEQRES 2 B 146 ILE PHE SER HIS MET ASP TYR ASP ASP ILE GLY PRO LYS SEQRES 3 B 146 ALA LEU SER ARG CYS LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG HIS PHE SER GLY PHE GLY ASN LEU TYR ASN ALA GLU SEQRES 5 B 146 ALA ILE ILE GLY ASN ALA ASN VAL ALA ALA HIS GLY ILE SEQRES 6 B 146 LYS VAL LEU HIS GLY LEU ASP ARG GLY VAL LYS ASN MET SEQRES 7 B 146 ASP ASN ILE ALA ALA THR TYR ALA ASP LEU SER THR LEU SEQRES 8 B 146 HIS SER GLU LYS LEU HIS VAL ASP PRO ASP ASN PHE LYS SEQRES 9 B 146 LEU LEU SER ASP CYS ILE THR ILE VAL LEU ALA ALA LYS SEQRES 10 B 146 MET GLY HIS ALA PHE THR ALA GLU THR GLN GLY ALA PHE SEQRES 11 B 146 GLN LYS PHE LEU ALA VAL VAL VAL SER ALA LEU GLY LYS SEQRES 12 B 146 GLN TYR HIS SEQRES 1 C 142 SER LEU SER ASP LYS ASP LYS ALA ALA VAL ARG ALA LEU SEQRES 2 C 142 TRP SER LYS ILE GLY LYS SER ALA ASP ALA ILE GLY ASN SEQRES 3 C 142 ASP ALA LEU SER ARG MET ILE VAL VAL TYR PRO GLN THR SEQRES 4 C 142 LYS THR TYR PHE SER HIS TRP PRO ASP VAL THR PRO GLY SEQRES 5 C 142 SER PRO HIS ILE LYS ALA HIS GLY LYS LYS VAL MET GLY SEQRES 6 C 142 GLY ILE ALA LEU ALA VAL SER LYS ILE ASP ASP LEU LYS SEQRES 7 C 142 THR GLY LEU MET GLU LEU SER GLU GLN HIS ALA TYR LYS SEQRES 8 C 142 LEU ARG VAL ASP PRO ALA ASN PHE LYS ILE LEU ASN HIS SEQRES 9 C 142 CYS ILE LEU VAL VAL ILE SER THR MET PHE PRO LYS GLU SEQRES 10 C 142 PHE THR PRO GLU ALA HIS VAL SER LEU ASP LYS PHE LEU SEQRES 11 C 142 SER GLY VAL ALA LEU ALA LEU ALA GLU ARG TYR ARG SEQRES 1 D 146 VAL GLU TRP THR ASP LYS GLU ARG SER ILE ILE SER ASP SEQRES 2 D 146 ILE PHE SER HIS MET ASP TYR ASP ASP ILE GLY PRO LYS SEQRES 3 D 146 ALA LEU SER ARG CYS LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG HIS PHE SER GLY PHE GLY ASN LEU TYR ASN ALA GLU SEQRES 5 D 146 ALA ILE ILE GLY ASN ALA ASN VAL ALA ALA HIS GLY ILE SEQRES 6 D 146 LYS VAL LEU HIS GLY LEU ASP ARG GLY VAL LYS ASN MET SEQRES 7 D 146 ASP ASN ILE ALA ALA THR TYR ALA ASP LEU SER THR LEU SEQRES 8 D 146 HIS SER GLU LYS LEU HIS VAL ASP PRO ASP ASN PHE LYS SEQRES 9 D 146 LEU LEU SER ASP CYS ILE THR ILE VAL LEU ALA ALA LYS SEQRES 10 D 146 MET GLY HIS ALA PHE THR ALA GLU THR GLN GLY ALA PHE SEQRES 11 D 146 GLN LYS PHE LEU ALA VAL VAL VAL SER ALA LEU GLY LYS SEQRES 12 D 146 GLN TYR HIS HET K 1001 1 HET K 1002 1 HET ACE A 0 3 HET ACE C 0 3 HET HEM A 200 43 HET HEM B 400 43 HET HEM C 600 43 HET HEM D 800 43 HETNAM K POTASSIUM ION HETNAM ACE ACETYL GROUP HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 K 2(K 1+) FORMUL 7 ACE 2(C2 H4 O) FORMUL 9 HEM 4(C34 H32 FE N4 O4) FORMUL 13 HOH *378(H2 O) HELIX 1 1 SER A 3 GLY A 18 1 16 HELIX 2 2 SER A 20 TYR A 36 1 17 HELIX 3 3 PRO A 37 SER A 44 5 8 HELIX 4 4 SER A 53 LYS A 73 1 21 HELIX 5 5 ASP A 76 LEU A 81 1 6 HELIX 6 6 LEU A 81 TYR A 90 1 10 HELIX 7 7 PRO A 96 PHE A 114 1 19 HELIX 8 8 THR A 119 ALA A 138 1 20 HELIX 9 9 THR B 4 MET B 18 1 15 HELIX 10 10 ASP B 19 TYR B 35 1 17 HELIX 11 11 PRO B 36 GLY B 46 5 11 HELIX 12 12 ASN B 50 GLY B 56 1 7 HELIX 13 13 ASN B 57 GLY B 70 1 14 HELIX 14 14 LEU B 71 LYS B 76 1 6 HELIX 15 15 ASN B 80 TYR B 85 1 6 HELIX 16 16 TYR B 85 LYS B 95 1 11 HELIX 17 17 ASP B 99 GLY B 119 1 21 HELIX 18 18 HIS B 120 PHE B 122 5 3 HELIX 19 19 THR B 123 LYS B 143 1 21 HELIX 20 20 SER C 3 GLY C 18 1 16 HELIX 21 21 SER C 20 TYR C 36 1 17 HELIX 22 22 PRO C 37 SER C 44 5 8 HELIX 23 23 SER C 53 LYS C 73 1 21 HELIX 24 24 ASP C 76 LEU C 81 1 6 HELIX 25 25 LEU C 81 LYS C 91 1 11 HELIX 26 26 PRO C 96 PHE C 114 1 19 HELIX 27 27 THR C 119 ALA C 138 1 20 HELIX 28 28 GLU C 139 ARG C 142 5 4 HELIX 29 29 THR D 4 MET D 18 1 15 HELIX 30 30 ASP D 19 TYR D 35 1 17 HELIX 31 31 PRO D 36 PHE D 42 5 7 HELIX 32 32 ASN D 50 GLY D 56 1 7 HELIX 33 33 ASN D 57 GLY D 70 1 14 HELIX 34 34 LEU D 71 ASN D 77 1 7 HELIX 35 35 ASN D 80 TYR D 85 1 6 HELIX 36 36 TYR D 85 LYS D 95 1 11 HELIX 37 37 PRO D 100 GLY D 119 1 20 HELIX 38 38 HIS D 120 PHE D 122 5 3 HELIX 39 39 THR D 123 GLY D 142 1 20 LINK NE2 HIS A 88 FE HEM A 200 LINK NE2 HIS B 92 FE HEM B 400 LINK NE2 HIS C 88 FE HEM C 600 LINK NE2 HIS D 92 FE HEM D 800 LINK C ACE A 0 N SER A 1 LINK C ACE C 0 N SER C 1 CRYST1 61.800 94.630 61.860 90.00 90.19 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.016181 0.000000 0.000054 0.00000 SCALE2 0.000000 0.010567 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016166 0.00000